The glycoproteins and other envelope proteins of two animal viruses, vesicular stomatitis virus (VSV) and Rauscher murine leukemia virus (RLV), will be studied. The isolated VSV glycoprotein possesses three of the virion-associated biological activities: antigenicity, hemagglutination and the inhibition of cellular macromolecular synthesis. Host-cell modification influences the hemagglutinating ability of the glycoprotein. Biological activities associated with RLV envelope proteins include antigenicity, hemagglutination, and possibly cell fusion. Some of the cell surface antigens of tumors and transformed cells are similar to RLV antigens. In order to do quantitative biological experiments, the VSV glycoprotein will be partially degraded to soluble glycopeptides. The native glycoprotein and the biologically active glycopeptides will be used to study virus-cell interactions and the effects that they have on cellular DNA, RNA and protein synthesis. Chemical analysis of the glycoprotein including amino acid composition, peptide mapping and end group analysis will be performed in order to determine the purity of the glycoprotein which has multiple biological activities. The number, size and sugar composition of the carbohydrate moieties will also be determined. The chemical composition of the non-glycosylated membrane protein will be analyzed in a similar manner. The envelope proteins of RLV will be isolated and purified. Biological and biochemical analyses, similar to those described for the VSV envelope proteins, will be performed on the RLV envelope proteins. Since glycoproteins of viruses and cells are important in the control of intercellular interactions and may play a role in the control of cellular macromolecular synthesis, the biological and biochemical studies on the viral envelope proteins which are described in this proposal should help elucidate the mechanism of action of the glycoproteins of normal and transformed cells.